› 4fkd

X-ray diffraction
1.63Å resolution

Identification of the Activator Binding Residues in the Second Cysteine-Rich Regulatory Domain of Protein Kinase C Theta

Released:
DOI: 10.2210/pdb4fkd/pdb
PDB entry 4fkd coloured by chain, front view.
PDB entry 4fkd coloured by chain, side view.
PDB entry 4fkd coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Identification of the activator-binding residues in the second cysteine-rich regulatory domain of protein kinase Cθ (PKCθ).
Rahman GM, Shanker S, Lewin NE, Kedei N, Hill CS, Prasad BV, Blumberg PM, Das J
Biochem J 451 33-44 (2013)
PMID: 23289588

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169669 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein kinase C theta type Chain: A
Molecule details ›
Chain: A
Length: 65 amino acids
Theoretical weight: 7.32 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q02111 (Residues: 232-281; Coverage: 7%)
Gene names: Pkcq, Prkcq
Sequence domains: Phorbol esters/diacylglycerol binding domain (C1 domain)
Structure domains: Wheat Germ Agglutinin (Isolectin 2); domain 1

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P61
Unit cell:
a: 65.85Å b: 65.85Å c: 27.12Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.173 0.171 0.204
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Plant phosphoinositide-dependent phospholipases C: variations around a canonical theme.
Pokotylo et al. (2014)
2 more

3 mentions without citation

Identification of the activator-binding residues in the second cysteine-rich regulatory domain of protein kinase Cθ (PKCθ).
Rahman et al. (2013)
2 more